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HPLC에 의한 분자량 결정에 저분자 표준단백질의 재평가
손희숙 전북대학교 유전공학연구소 1988 遺傳工學硏究所報 Vol.1 No.1
Reevaluation of protein standards which have been used in conventional gel filtration chromatography was conducted by high performance gel filtration column. Plotting the log molecular weight and its retention time, a linear calibration curve could be achieved using the well documented protein standards. However, an unexpected finding was the deviation of several protein standards approximately ranging from 13,000 to 15,000 from linearity. Although we did not clarify the question about the deviation of cytochrome C, lysozyme, ribonuclease A, and α-lactalbumin, we assume that the physico-chemical differences between two matrices, PROTEIN-PAK 125 and Sephadex G-75, may explain this behaviour.
Bacillus 균이 생산하는 구성효소로서의 이눌라아제
홍재식,변시명,엄태붕,손희숙,박문국 한국농화학회 1985 Applied Biological Chemistry (Appl Biol Chem) Vol.28 No.3
Recently, we investigated characteristics of a bacterium which has never been reported as an inulin hydrolyzing microorganism. Several properties of the isolated microorganism were aerobic, rod typed, spore forming and Gram positive. According to the Bergey's manual, this bacterium tentatively appeared to be Bacillum subtilis. This bacterium produced inulase constitutively in the media containing glucose, sucrose or cellulose without inulin as a sole carbon source. Also, inulase activities of the bacterium per unit culture volume showed 1.1 unit/㎖ comparable to 0.9 unit/㎖ of Kluyveromyces fragilis with a relatively short culture time.
Aspergillus ficuum 조효소액으로부터 Endoinulinase의 정제 및 특성
한상배,유향숙,노민환,이태규,손희숙,우순자,엄태붕 한국산업미생물학회 1991 한국미생물·생명공학회지 Vol.19 No.2
Aspergillus ficuum이 생산하는 endoglycosidase가 conventional CM, DEAE 및 HPLC DEAE, gel chromatography에 의해 단백질 ㎎당 460±40U의 specific activity로 정제되었다. 이 효소는 약 72,000분자량을 가지는 단량체로 이루어져 있었으며 당을 함유하고 있었다. 분해산물의 조사에 의한 작용기작은 전형적 endo cleavage mode를 보여주었으며 특이하게도 sucrose와 palatinose를 분해할 수 있었다. Endoinulinase was purified from a commercial inulin preparation produced by Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAE-Sepharose 6B, HPLC gel filtration on a Protein Pak 125 Column and HPLC ion exchange chromatography on a TSK DEAE-5pw Column. The endoinulinase had a molecular weight of 72,000±1,000 and was glycoprotein with 23 to 25% w/w sugar content. The enzyme was much more active on inulin with random cleavage mode than on sucrose and on palatinose: The ratio of activity on inulin and sucrose (I/S ratio) was 10∼14.
Vinylsulfone Activated Agarose에 Endo- 및 Exoinulinase의 고정화
한상배,송근섭,정용섭,손희숙,우순자,엄태붕 한국산업미생물학회 1992 한국미생물·생명공학회지 Vol.20 No.1
Inulinase의 효율적인 재사용을 위하여 vinylsulfone activated agarose에 endo- 및 exoinulinase를 고정화시켰다. Gram gel당 exoinulinase는 400U, endoinulinase는 80U까지 고정화시킬 수가 있었고 열 안정성은 exoinulinase에서 증가되었다. 두 고정화 효소의 혼합비율에 따른 synergistic effect는 endo/exo가 0.5∼O.1일 때 가장 컸으며, synergistic effect는 혼합되지 않은 상태의 고정화 효소에 비해 그 활성이 약 1.7배 증가하였다. 두 고정화 효소의 최적 pH는 4.4∼5.0 범위이었으며 operational stability는 batch reactor에서 20번 반복된 실험결과 어떠한 효소활성의 감소도 보이지 않았다. In order to reuse inulinase effectively, a method for immobilizing both endo- and exoinulinase to vinylsulfone activated agarose via covalent bond was investigated. The immobilized enzyme preparation had, respectively, 400 U for exoinulinase activity and 80 U for endoinulinase activity per gram gel. A thermal stability by immobilization had increased in the case of exoinulinase. Optimum pHs for two immobilized enzymes were 4.4 to 5.0. Synergistic effect which depends on mixed ratio of two immobilized enzymes was the best when the mixed ratio of endo/exo lay between 0.1 and 0.5, and its activity of the mixed enzyme increased 1.7 times as compared to that of each immobilized enzyme. Inulinase activities of both of the immobilized enzymes did not change during 20 times experimental runs in a batch reactor.
Aspergillus ficuum 조효소액으로부터 Exoinulinase의 정제 및 특성
한상배,송근섭,유향숙,노민환,이태규,손희숙,우순자,엄태붕 한국산업미생물학회 1991 한국미생물·생명공학회지 Vol.19 No.3
Aspergillus ficuum이 생산하는 exoinulinase가 CM-Sephadex, DEAE-Sepharose 6B 및 HPLC gel filtration을 통해 단백질 ㎎당 약 2,800U의 specific activity로 정제되었다. 이 효소는 native 상태에서 약 83,000±1,000의 분자량을 나타냈으며 당을 함유하고 있었다. 이 효소는 최적 pH가 4.4∼4.7이었고 55℃에서 8시간 노출 후에도 그 활성을 95% 유지하였다. 이 효소의 I/S ratio는 약 0.35이고 전형적인 non-speific β-fructofuranosidase의 특성을 나타내었으며 raffinose와 stachyose를 분해할 수 있었다. An exoinulinase (EC 3.2.1.80) was purified from a commercial inulinase preparation from Aspergillus ficuum using ion exchange chromatography on CM-Sephadex C-50 and DEAE-Sepharose 6B and HPLC gel filtration on a Protein Pak 125 column. Native exoinulinase had a molecular weight of 83,000±1,000 and was glycoprotein. Optimal pHs of the enzyme were ranged from 4.4 to 4.7. About ninety five percent of the whole activity was maintained even after incubation of 8 hours at 55℃. The enzyme was a typical non-specific β-fructofuranosidase, of which I/S ratio appears to be 0.35.